ID   PP14A_RAT               Reviewed;         147 AA.
AC   Q99MC0;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 14A;
DE   AltName: Full=17 kDa PKC-potentiated inhibitory protein of PP1;
DE   AltName: Full=Protein kinase C-potentiated inhibitor protein of 17 kDa;
DE            Short=CPI-17;
GN   Name=Ppp1r14a; Synonyms=Cpi, Cpi17;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yu L.;
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Smooth muscle;
RX   PubMed=12974676; DOI=10.1042/bj20030128;
RA   Liu Q.-R., Zhang P.-W., Lin Z., Li Q.-F., Woods A.S., Troncoso J.,
RA   Uhl G.R.;
RT   "GBPI, a novel gastrointestinal- and brain-specific PP1-inhibitory protein,
RT   is activated by PKC and inactivated by PKA.";
RL   Biochem. J. 377:171-181(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-128 AND SER-136, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory
CC       activity when phosphorylated, creating a molecular switch for
CC       regulating the phosphorylation status of PPP1CA substrates and smooth
CC       muscle contraction (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP1 inhibitor family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF352572; AAK35213.1; -; mRNA.
DR   EMBL; AY050673; AAL25831.1; -; mRNA.
DR   RefSeq; NP_569087.1; NM_130403.1.
DR   RefSeq; XP_017444133.1; XM_017588644.1.
DR   AlphaFoldDB; Q99MC0; -.
DR   SMR; Q99MC0; -.
DR   STRING; 10116.ENSRNOP00000028070; -.
DR   iPTMnet; Q99MC0; -.
DR   PhosphoSitePlus; Q99MC0; -.
DR   PaxDb; Q99MC0; -.
DR   PRIDE; Q99MC0; -.
DR   GeneID; 114004; -.
DR   KEGG; rno:114004; -.
DR   UCSC; RGD:620536; rat.
DR   CTD; 94274; -.
DR   RGD; 620536; Ppp1r14a.
DR   VEuPathDB; HostDB:ENSRNOG00000020676; -.
DR   eggNOG; ENOG502S2I4; Eukaryota.
DR   HOGENOM; CLU_114155_2_0_1; -.
DR   InParanoid; Q99MC0; -.
DR   OMA; LHKQPGF; -.
DR   OrthoDB; 1492626at2759; -.
DR   PhylomeDB; Q99MC0; -.
DR   TreeFam; TF105546; -.
DR   Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR   PRO; PR:Q99MC0; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020676; Expressed in testis and 20 other tissues.
DR   Genevisible; Q99MC0; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; TAS:RGD.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR   GO; GO:0042325; P:regulation of phosphorylation; IEA:InterPro.
DR   Gene3D; 1.10.150.220; -; 1.
DR   InterPro; IPR008025; CPI-17.
DR   InterPro; IPR036658; CPI-17_sf.
DR   PANTHER; PTHR16188; PTHR16188; 1.
DR   Pfam; PF05361; PP1_inhibitor; 1.
DR   SUPFAM; SSF81790; SSF81790; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Protein phosphatase inhibitor;
KW   Reference proteome.
FT   CHAIN           1..147
FT                   /note="Protein phosphatase 1 regulatory subunit 14A"
FT                   /id="PRO_0000071489"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..120
FT                   /note="Inhibitory"
FT   REGION          118..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..147
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         38
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A00"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A00"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   147 AA;  16697 MW;  116B39AA2FA1CD12 CRC64;
     MAAQRLGKRV LSKLQSPSRA RGPGGSPSGL QKRHARVTVK YDRRELQRRL DVEKWIDGRL
     EELYRGREAD MPDEVNIDEL LELDSEEERC RKIRGLLEAC LNPTEDFVQE LLAKLRGLHK
     QPGFPQPSPS DDPSLSPRQD PAHTAPP